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Literature summary extracted from

  • Belinskaya, T.; Pattabiraman, N.; diTargiani, R.; Choi, M.; Saxena, A.
    Differences in amino acid residues in the binding pockets dictate substrate specificities of mouse senescence marker protein-30, human paraoxonase1, and squid diisopropylfluorophosphatase (2012), Biochim. Biophys. Acta, 1824, 701-710.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.8.2 homology modeling and docking of substrates. The two identical hydrophobic isopropyl groups in diisopropyl fluorophosphate bind to two different sub-pockets in the binding-site. Sub-pocket 1 is formed by residues P36, E37, I72, A74 and M90 while sub-pocket 2 is formed by F173, N175, T195, and W244 Loligo vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Loligo vulgaris Q7SIG4
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.8.2 82
-
 substrate soman, pH 8.0, temperature not specified in the publication Loligo vulgaris
3.1.8.2 110
-
 substrate sarin, pH 8.0, temperature not specified in the publication Loligo vulgaris
3.1.8.2 198
-
 substrate cyclosarin, pH 8.0, temperature not specified in the publication Loligo vulgaris
3.1.8.2 225
-
 substrate diisopropyl fluorophosphate, pH 8.0, temperature not specified in the publication Loligo vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 cyclosarin + H2O
-
 Loligo vulgaris ?
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Loligo vulgaris diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 sarin + H2O
-
 Loligo vulgaris ?
-
 ?
3.1.8.2 soman + H2O
-
 Loligo vulgaris ?
-
 ?